Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Pascale Bomont"'
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 11 (2023)
Neurofilaments (NFs) are the most abundant component of mature neurons, that interconnect with actin and microtubules to form the cytoskeleton. Specifically expressed in the nervous system, NFs present the particularity within the Intermediate Filame
Externí odkaz:
https://doaj.org/article/154af11694d241a1b72923f9d03849da
Publikováno v:
EMBO Molecular Medicine, Vol 15, Iss 7, Pp 1-19 (2023)
Abstract Giant axonal neuropathy (GAN) is a fatal neurodegenerative disorder for which there is currently no treatment. Affecting the nervous system, GAN starts in infancy with motor deficits that rapidly evolve toward total loss of ambulation. Using
Externí odkaz:
https://doaj.org/article/e65f099e7b7d4a7eb50038ba56f7b508
Publikováno v:
Cells, Vol 13, Iss 1, p 103 (2024)
Autophagy is a major degradative pathway that plays a key role in sustaining cell homeostasis, integrity, and physiological functions. Macroautophagy, which ensures the clearance of cytoplasmic components engulfed in a double-membrane autophagosome t
Externí odkaz:
https://doaj.org/article/c669293e4a2d41a290136e5547494c74
Publikováno v:
Frontiers in Molecular Neuroscience, Vol 15 (2022)
The zebrafish (Danio rerio) is a vertebrate species offering multitude of advantages for the study of conserved biological systems in human and has considerably enriched our knowledge in developmental biology and physiology. Being equally important i
Externí odkaz:
https://doaj.org/article/0b05e9437eab4314a2e19354a1b3534b
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
Membrane elongation is fundamental to autophagy and is controlled by an ubiquitin-conjugating cascade orchestrated by ATG16L1. Here, the authors identify that the E3 ligase Gigaxonin regulates autophagosome formation by controlling ATG16L1 turnover.
Externí odkaz:
https://doaj.org/article/2e1c17d96cec4e74b80786a4cfe81395
Autor:
Léa Lescouzères, Pascale Bomont
Publikováno v:
Frontiers in Physiology, Vol 11 (2020)
Ubiquitination is a dynamic post-translational modification that regulates the fate of proteins and therefore modulates a myriad of cellular functions. At the last step of this sophisticated enzymatic cascade, E3 ubiquitin ligases selectively direct
Externí odkaz:
https://doaj.org/article/aeb8bf0dec93418992c224bb3cde6da8
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
Autophagy is an essential self-digestion machinery for cell survival and homoeostasis. Membrane elongation is fundamental, as it drives the formation of the double-membrane vesicles that engulf cytosolic material. LC3-lipidation, the signature of aut
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f87bb30abdef244520c645b21fb5bc6a
https://doaj.org/article/2e1c17d96cec4e74b80786a4cfe81395
https://doaj.org/article/2e1c17d96cec4e74b80786a4cfe81395
Autor:
Pascale Bomont, Léa Lescouzères
Publikováno v:
Frontiers in Physiology, Vol 11 (2020)
Frontiers in Physiology
Frontiers in Physiology
Ubiquitination is a dynamic post-translational modification that regulates the fate of proteins and therefore modulates a myriad of cellular functions. At the last step of this sophisticated enzymatic cascade, E3 ubiquitin ligases selectively direct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ca7d953946f5ee7a863d8530fbcad46
https://www.frontiersin.org/articles/10.3389/fphys.2020.01022/full
https://www.frontiersin.org/articles/10.3389/fphys.2020.01022/full
Autor:
Pascale, Bomont
Publikováno v:
Current opinion in cell biology. 68
In the last two years, neurofilaments (NFs) have become one of the most blazing topics in clinical neuroscience. NFs are major cytoskeletal constituents of neurons, can be detected in body fluids, and have recently emerged as universal biomarkers of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::da4dca86253b0b349a2b220bb928012d
https://pubmed.ncbi.nlm.nih.gov/33454158
https://pubmed.ncbi.nlm.nih.gov/33454158